The dynamics of an enzyme may be vital to its recognition and action on a substrate. NMR can be used to probe the dynamics of specific location in a protein. I have used NMR to determine the dynamics of the backbone amides of alpha-lytic protease, a bacterial extracellular serine protease of 198 amino acids. I used a new technique of converting NMR relaxation data into dynamics called "Reduced Spectral Density Mapping". The binding pocket of the enzyme has a great deal of dynamic activity, which is stabilized by the presence of a peptide boronic acid inhibitor which mimics the transition state. The pattern of dynamics and stabilization suggests that dynamics may play a role in allowing non-specific binding of substrate residues that are away from the cleavage position. I used MidasPlus to display the molecule and observe the patterns of dynamics, and their possible role in substrate recognition and binding specificity. I also used the Computer Graphics Laboratory programs to determine solvent accessible surfaces.